Phosphotyrosine antibody

Details for Product No. ABIN863079
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Antigen
Reactivity
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(166), (46), (32), (28), (16), (10), (8), (8), (4), (1), (1), (1), (1)
Host
Mouse
(185), (48), (2)
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
(28), (21), (18), (7), (6), (5), (4), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Application
Western Blotting (WB), Immunoprecipitation (IP), Immunofluorescence (IF), Immunohistochemistry (IHC)
(168), (110), (91), (33), (32), (28), (28), (16), (15), (10), (3), (1), (1), (1)
Pubmed 8 references available
Quantity 100 µg
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Catalog No. ABIN863079
355.30 $
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Immunogen Phosphotyrosine alanine and glyceine in a 1:1:1 ratio polymerized in the presence of keyhole limpet hemocyanin with 1-ethyl-3-(3'-dimentrylaminopropyl) carbodiimide.
Clone G104
Isotype IgG1
Specificity Approx. 38 kDa. Can run up to 4 5 kDa on SDS Page
Cross-Reactivity (Details) Does not cross-react with phosphoserine or phosphothreonine.
Sensitivity 1 µg/mL of SMC-174 was sufficient for detection of phosphorylated tyrosine residues in 10 µg of rat tissue lysate by colorimetric immunoblot analysis using Goat anti-rat IgG:HRP as the secondary antibody.
Purification Protein G Purified
Background Protein phosphorylation is an important posttranslational modification that serves many key functions to regulate a protein’s activity, localization, and protein-protein interactions. Phosphorylation is catalyzed by various specific protein kinases, which involves removing a phosphate group from ATP and covalently attaching it to to a recipient protein that acts as a substrate. Most kinases act on both serine and threonine, others act on tyrosine, and a number (dual specificity kinases) act on all three. Because phosphorylation can occur at multiple sites on any given protein, it can therefore change the function or localization of that protein at any time.Changing the function of these proteins has been linked to a number of diseases, including cancer, diabetes, heart disease, inflammation and neurological disorders.In particular, the phosphorylation of tyrosine is considered one of the key steps in signal transduction and regulation of enzymatic activity. Phosphotyrosine can be detected through specific antibodies, and are helpful in facilitating the identification of tyrosine kinase substrates.
Research Area Signaling, Metabolism, Amino Acids, Protein Modifications, Cell Signaling
Application Notes Recommended Dilution: 1:1000 (WB)
Restrictions For Research Use only
Concentration 1 mg/mL
Buffer PBS pH 7.4, 50 % glycerol, 0.09 % sodium azide
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Supplier Images
anti-Phosphotyrosine antibody P Tyrosine.
Background publications Ross, Baltimore, Eisen: "Phosphotyrosine-containing proteins isolated by affinity chromatography with antibodies to a synthetic hapten." in: Nature, Vol. 294, Issue 5842, pp. 654-6, 1982 (PubMed).

Garton, Flint, Tonks: "Identification of p130(cas) as a substrate for the cytosolic protein tyrosine phosphatase PTP-PEST." in: Molecular and cellular biology, Vol. 16, Issue 11, pp. 6408-18, 1996 (PubMed).

Garton, Tonks: "Regulation of fibroblast motility by the protein tyrosine phosphatase PTP-PEST." in: The Journal of biological chemistry, Vol. 274, Issue 6, pp. 3811-8, 1999 (PubMed).

Pawson, Saxton: "Signaling networks--do all roads lead to the same genes?" in: Cell, Vol. 97, Issue 6, pp. 675-8, 1999 (PubMed).

Tiganis, Kemp, Tonks: "The protein-tyrosine phosphatase TCPTP regulates epidermal growth factor receptor-mediated and phosphatidylinositol 3-kinase-dependent signaling." in: The Journal of biological chemistry, Vol. 274, Issue 39, pp. 27768-75, 1999 (PubMed).

Blume-Jensen, Hunter: "Oncogenic kinase signalling." in: Nature, Vol. 411, Issue 6835, pp. 355-65, 2001 (PubMed).

Downward: "The ins and outs of signalling." in: Nature, Vol. 411, Issue 6839, pp. 759-62, 2001 (PubMed).

Goto, Kiyono, Tomono et al.: "Complex formation of Plk1 and INCENP required for metaphase-anaphase transition." in: Nature cell biology, Vol. 8, Issue 2, pp. 180-7, 2006 (PubMed).

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